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Database: UniProt
Entry: G8PE62_PEDCP
LinkDB: G8PE62_PEDCP
Original site: G8PE62_PEDCP 
ID   G8PE62_PEDCP            Unreviewed;       825 AA.
AC   G8PE62;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:AEV95547.1};
GN   Name=clpC {ECO:0000313|EMBL:AEV95547.1};
GN   OrderedLocusNames=PECL_1315 {ECO:0000313|EMBL:AEV95547.1};
OS   Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS   3811 / P06).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95547.1, ECO:0000313|Proteomes:UP000005444};
RN   [1] {ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV95547.1, ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RX   PubMed=22328764; DOI=10.1128/JB.06759-11;
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   J. Bacteriol. 194:1271-1272(2012).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP003137; AEV95547.1; -; Genomic_DNA.
DR   RefSeq; WP_014215741.1; NC_016605.1.
DR   AlphaFoldDB; G8PE62; -.
DR   STRING; 701521.PECL_1315; -.
DR   KEGG; pce:PECL_1315; -.
DR   PATRIC; fig|701521.8.peg.1226; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000005444; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:AEV95547.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEV95547.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005444};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          425..460
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          151..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          421..448
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        153..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  91197 MW;  03BF94BDAD3785DD CRC64;
     MDNLFTPSAK NVLMIAQEQA KKFKHPAVGT EHLLLALTIE QNGVAKSVLD QFNVQEVDVT
     EEIESFTGYG NLTSRKNDYL PYSPKAKEIL SLAGDEAKQL KSSKIGTEHL LLALLQDDSI
     LSSRILAALD ISVSDVQKVA LRKLGVNPAV RARQARQRQT NGGQSSATPT LDSVARDLTE
     MAAEGQIDPV VGRSKEVRRV IQILSRRTKN NPVLIGEPGV GKTAIAEGLA QRIVDGDVPE
     DMQNKRLMML EMGSLVAGTK YRGEFEDRLK KVIEEIRTDK GIILFIDELH TLIGAGGAEG
     AIDASNILKP ALARGELQTI GATTLNEYQK YIESDAALER RFARVEVNEP TEDEAIQILK
     GLRGKYEEHH HVEITDEAIV EAVKLSSRYI SDRYLPDKAI DLIDEAAAKI RIDGSEKPDS
     KSKNEAKLAE LRQEKEDAID AQEFEKAATI REKEFKLAKK VEKQNNDSEK ADSKNEYDLV
     ETAESVAEIV SDWTGVPLTH LEQAESDRLI NLEKTLHERV IGQDEAVSAV ARAIRRARSG
     LKDPKRPIGS FMFLGPTGVG KTELAKTLAD VMFGSEDNMI RIDMSEYMER YSTSRLVGSA
     PGYVGYDEGG QLTEQVRRKP YSVVLFDEVE KAHPDVFNLL LQVLDDGFLT DSKGRRVDFR
     NTILIMTSNL GATALRDEKS VGFAAKNASE DYNAMSAKVR EILKQSFRPE FLNRIDETII
     FHSLTKEELH SIVKLMAKDV ILRMSEQGIN TKLTPAAIDA VADAGFDPEF GARPIRRALQ
     TDVEDKLSEL ILSGEATVGD DVTVGARNGK ITFKVSSVQK NKVNN
//
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